TRPF_HAHCH
ID TRPF_HAHCH Reviewed; 213 AA.
AC Q2SJD2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000255|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000255|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000255|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000255|HAMAP-Rule:MF_00135}; OrderedLocusNames=HCH_02435;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000255|HAMAP-Rule:MF_00135};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000255|HAMAP-
CC Rule:MF_00135}.
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DR EMBL; CP000155; ABC29242.1; -; Genomic_DNA.
DR RefSeq; WP_011396311.1; NC_007645.1.
DR AlphaFoldDB; Q2SJD2; -.
DR SMR; Q2SJD2; -.
DR STRING; 349521.HCH_02435; -.
DR PRIDE; Q2SJD2; -.
DR EnsemblBacteria; ABC29242; ABC29242; HCH_02435.
DR KEGG; hch:HCH_02435; -.
DR eggNOG; COG0135; Bacteria.
DR HOGENOM; CLU_076364_2_0_6; -.
DR OMA; FYAKSPR; -.
DR OrthoDB; 1854712at2; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Isomerase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..213
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT /id="PRO_1000095923"
SQ SEQUENCE 213 AA; 23313 MW; D1974AD5C2FAA055 CRC64;
MTARNKRVRC KICGILELEH ALAVSDAGGD AIGFVFYPPS PRYIDPAAAS RIIAKLPPFI
TTVGLFVNHS AEQVREILNV VPLDVLQFHG NEDNDFCRSF SRPFYKAIGV GDETDVVAEA
AKYPDAAALL FDTHDPQLRG GTGRVFDWSR IRHELGKPVI LAGGLNPTNV AEAIRTVRPY
AVDVSGGVEA SKGVKSIELI QEFIGEVYRE YEV